Altering of the metal specificity of Escherichia coli alkaline phosphatase.
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Coordination sphere of the third metal site is essential to the activity and metal selectivity of alkaline phosphatasesX-Ray Structure Reveals a New Class and Provides Insight into Evolution of Alkaline PhosphatasesStructural and Mechanistic Insights into C-P Bond Hydrolysis by Phosphonoacetate HydrolaseEvolution of bacterial phosphoglycerate mutases: non-homologous isofunctional enzymes undergoing gene losses, gains and lateral transfersProteins adopt functionally active conformations after type III secretionEffects of replacing active site residues in a cold-active alkaline phosphatase with those found in its mesophilic counterpart from Escherichia coli.
P2860
Altering of the metal specificity of Escherichia coli alkaline phosphatase.
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Altering of the metal specificity of Escherichia coli alkaline phosphatase.
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Altering of the metal specificity of Escherichia coli alkaline phosphatase.
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type
label
Altering of the metal specificity of Escherichia coli alkaline phosphatase.
@en
Altering of the metal specificity of Escherichia coli alkaline phosphatase.
@nl
prefLabel
Altering of the metal specificity of Escherichia coli alkaline phosphatase.
@en
Altering of the metal specificity of Escherichia coli alkaline phosphatase.
@nl
P2860
P356
P1476
Altering of the metal specificity of Escherichia coli alkaline phosphatase.
@en
P2093
Cheryl L Wojciechowski
Evan R Kantrowitz
P2860
P304
50476-50481
P356
10.1074/JBC.M209326200
P407
P577
2002-10-23T00:00:00Z